KLHDB_DROME
ID KLHDB_DROME Reviewed; 623 AA.
AC Q9VUU5; Q9NGX7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Kelch-like protein diablo {ECO:0000312|EMBL:BAD06413.1};
GN Name=dbo {ECO:0000312|EMBL:AAF49578.1, ECO:0000312|FlyBase:FBgn0040230};
GN ORFNames=CG6224;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:BAD06413.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamashita A., Togashi S.;
RT "Drosophila kelch-like protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAD06413.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stuart B.D., Wasserman S.A.;
RT "Identification of Diablo, a new Drosophila melanogaster Kelch family
RT protein.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAF49578.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF49578.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:BAD06413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23590.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16408305; DOI=10.1002/neu.20229;
RA Liebl F.L.W., Werner K.M., Sheng Q., Karr J.E., McCabe B.D.,
RA Featherstone D.E.;
RT "Genome-wide P-element screen for Drosophila synaptogenesis mutants.";
RL J. Neurobiol. 66:332-347(2006).
RN [7] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity). May have a
CC role in synapse differentiation and growth.
CC {ECO:0000250|UniProtKB:Q9Y2M5, ECO:0000269|PubMed:16408305}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9Y2M5}.
CC -!- DISRUPTION PHENOTYPE: Defects in synapse differentiation and growth;
CC undergrowth resulting in reduced numbers of boutons and/or branches.
CC {ECO:0000269|PubMed:16408305}.
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DR EMBL; AB027612; BAD06413.1; -; mRNA.
DR EMBL; AF237711; AAF43447.1; -; mRNA.
DR EMBL; AE014296; AAF49578.1; -; Genomic_DNA.
DR EMBL; BT010272; AAQ23590.1; -; mRNA.
DR RefSeq; NP_524989.2; NM_080250.3.
DR AlphaFoldDB; Q9VUU5; -.
DR SMR; Q9VUU5; -.
DR BioGRID; 72788; 6.
DR IntAct; Q9VUU5; 8.
DR STRING; 7227.FBpp0075260; -.
DR iPTMnet; Q9VUU5; -.
DR PaxDb; Q9VUU5; -.
DR PRIDE; Q9VUU5; -.
DR DNASU; 53556; -.
DR EnsemblMetazoa; FBtr0075505; FBpp0075260; FBgn0040230.
DR GeneID; 53556; -.
DR KEGG; dme:Dmel_CG6224; -.
DR UCSC; CG6224-RA; d. melanogaster.
DR CTD; 53556; -.
DR FlyBase; FBgn0040230; dbo.
DR VEuPathDB; VectorBase:FBgn0040230; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000155161; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; Q9VUU5; -.
DR OrthoDB; 731760at2759; -.
DR PhylomeDB; Q9VUU5; -.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9VUU5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 53556; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 53556; -.
DR PRO; PR:Q9VUU5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040230; Expressed in wing disc and 68 other tissues.
DR ExpressionAtlas; Q9VUU5; baseline and differential.
DR Genevisible; Q9VUU5; DM.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Kelch repeat; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..623
FT /note="Kelch-like protein diablo"
FT /id="PRO_0000379948"
FT DOMAIN 72..139
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 174..276
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REPEAT 323..369
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 371..417
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 418..464
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 466..511
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 513..558
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 559..605
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 286
FT /note="A -> V (in Ref. 2; AAF43447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 68923 MW; DCD75E9F66BBC6B9 CRC64;
MGDLPGSGST AQPRDAAVTG TGGNSTAGGG SSVGSTAVDR PPSPARLSHT SEKHPKVTLT
ELNMLRRHRE LCDVVLNVGG RKIFAHRVIL SACSSYFCAM FTGELEESRQ TEVTIRDIDE
NAMELLIDFC YTAHIIVEES NVQTLLPAAC LLQLVEIQDI CCEFLKRQLD PTNCLGIRAF
ADTHSCRELL RIADKFTQHN FQEVMESEEF LLLPVGQLVD IICSDELNVR SEEQVFNAVM
SWLKYNVAER RQHLAQVLQH VRLPLLSPKF LVGTVGSDLL VRSDEACRDL VDEAKNYLLL
PQERPLMQGP RTRPRKPTRR GEVLFAVGGW CSGDAIASVE RFDPQTNDWK MVAPMSKRRC
GVGVAVLNDL LYAVGGHDGQ SYLNSIERYD PQTNQWSCDV APTTSCRTSV GVAVLDGFLY
AVGGQDGVQC LNHVERYDPK ENKWSKVAPM TTRRLGVAVA VLGGFLYAIG GSDGQCPLNT
VERYDPRHNK WVAVSPMSTR RKHLGCAVFN NYIYAVGGRD DCMELSSAER YNPLTNTWSP
IVAMTSRRSG VGLAVVNGQL YAVGGFDGSA YLKTIEVYDP ETNQWRLCGC MNYRRLGGGV
GVMRAPQTEN YMWCENSFKQ PNS
